Binding of poly(amidoamine), carbosilane, phosphorus and hybrid dendrimers to thrombin—Constants and mechanisms
[Display omitted] •Dendrimers rearranged thrombin structure.•Flexible dendrimers increased unstructured state of thrombin.•Rigid dendrimers increased a number of beta-sheets of thrombin.•Parameters of binding differed using CD or fluorescence. Thrombin is an essential part of the blood coagulation s...
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Published in | Colloids and surfaces, B, Biointerfaces Vol. 155; pp. 11 - 16 |
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Main Authors | , , , , , , , , , , , , , , |
Format | Journal Article |
Language | English |
Published |
Netherlands
Elsevier B.V
01.07.2017
Elsevier |
Subjects | |
Online Access | Get full text |
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Summary: | [Display omitted]
•Dendrimers rearranged thrombin structure.•Flexible dendrimers increased unstructured state of thrombin.•Rigid dendrimers increased a number of beta-sheets of thrombin.•Parameters of binding differed using CD or fluorescence.
Thrombin is an essential part of the blood coagulation system; it is a serine protease that converts soluble fibrinogen into insoluble strands of fibrin, and catalyzes many other coagulation-related reactions. Absorption at its surface of small nanoparticles can completely change the biological properties of thrombin. We have analyzed the influence on thrombin of 3 different kinds of small nanoparticles: dendrimers (phosphorus-based, carbosilane based and polyamidoamine) and 2 hybrid systems containing carbosilane, viologen and phosphorus dendritic scaffolds in one single molecule, bearing different flexibility, size and surface charge. There was significant alteration in the rigidity of the rigid dendrimers in contrast to flexible dendrimers. These differences in their action are important in understanding interactions taking place at a bio-nanointerface. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0927-7765 1873-4367 |
DOI: | 10.1016/j.colsurfb.2017.03.053 |